Gene TPR - ENSG00000047410 | NCBI Gene ID: 7175

Details for: TPR

Gene ID: 7175

Symbol: TPR

Ensembl ID: ENSG00000047410

Description: translocated promoter region, nuclear basket protein

Associated with

Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to heat stress
(R-HSA-3371556)
Cytokine signaling in immune system
(R-HSA-1280215)
Defective tpr may confer susceptibility towards thyroid papillary carcinoma (tpc)
(R-HSA-5619107)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Disorders of transmembrane transporters
(R-HSA-5619115)
Export of viral ribonucleoproteins from nucleus
(R-HSA-168274)
Gene expression (transcription)
(R-HSA-74160)
Gene silencing by rna
(R-HSA-211000)
Glucose metabolism
(R-HSA-70326)
Glycolysis
(R-HSA-70171)
Hcmv early events
(R-HSA-9609690)
Hcmv infection
(R-HSA-9609646)
Hcmv late events
(R-HSA-9610379)
Hiv infection
(R-HSA-162906)
Hiv life cycle
(R-HSA-162587)
Host interactions of hiv factors
(R-HSA-162909)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Influenza viral rna transcription and replication
(R-HSA-168273)
Interactions of rev with host cellular proteins
(R-HSA-177243)
Interactions of vpr with host cellular proteins
(R-HSA-176033)
Interferon signaling
(R-HSA-913531)
Isg15 antiviral mechanism
(R-HSA-1169408)
Late phase of hiv life cycle
(R-HSA-162599)
Metabolism
(R-HSA-1430728)
Metabolism of carbohydrates
(R-HSA-71387)
Metabolism of non-coding rna
(R-HSA-194441)
Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Mitotic prophase
(R-HSA-68875)
M phase
(R-HSA-68886)
Nep/ns2 interacts with the cellular export machinery
(R-HSA-168333)
Ns1 mediated effects on host pathways
(R-HSA-168276)
Nuclear envelope breakdown
(R-HSA-2980766)
Nuclear import of rev protein
(R-HSA-180746)
Nuclear pore complex (npc) disassembly
(R-HSA-3301854)
Post-translational protein modification
(R-HSA-597592)
Processing of capped intron-containing pre-mrna
(R-HSA-72203)
Regulation of glucokinase by glucokinase regulatory protein
(R-HSA-170822)
Regulation of hsf1-mediated heat shock response
(R-HSA-3371453)
Rev-mediated nuclear export of hiv rna
(R-HSA-165054)
Sars-cov-2 activates/modulates innate and adaptive immune responses
(R-HSA-9705671)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov-2-host interactions
(R-HSA-9705683)
Sars-cov infections
(R-HSA-9679506)
Signaling by alk fusions and activated point mutants
(R-HSA-9725370)
Signaling by alk in cancer
(R-HSA-9700206)
Slc transporter disorders
(R-HSA-5619102)
Snrnp assembly
(R-HSA-191859)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of chromatin organization proteins
(R-HSA-4551638)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
Sumoylation of dna replication proteins
(R-HSA-4615885)
Sumoylation of rna binding proteins
(R-HSA-4570464)
Sumoylation of sumoylation proteins
(R-HSA-4085377)
Sumoylation of ubiquitinylation proteins
(R-HSA-3232142)
Transcriptional regulation by small rnas
(R-HSA-5578749)
Transport of mature mrna derived from an intron-containing transcript
(R-HSA-159236)
Transport of mature mrna derived from an intronless transcript
(R-HSA-159231)
Transport of mature mrnas derived from intronless transcripts
(R-HSA-159234)
Transport of mature transcript to cytoplasm
(R-HSA-72202)
Transport of ribonucleoproteins into the host nucleus
(R-HSA-168271)
Transport of the slbp dependant mature mrna
(R-HSA-159230)
Transport of the slbp independent mature mrna
(R-HSA-159227)
Trna processing
(R-HSA-72306)
Trna processing in the nucleus
(R-HSA-6784531)
Viral infection pathways
(R-HSA-9824446)
Viral messenger rna synthesis
(R-HSA-168325)
Vpr-mediated nuclear import of pics
(R-HSA-180910)
Chromatin binding
(GO:0003682)
Dynein complex binding
(GO:0070840)
Heat shock protein binding
(GO:0031072)
Mitogen-activated protein kinase binding
(GO:0051019)
Mrna binding
(GO:0003729)
Mrna export from nucleus
(GO:0006406)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nuclear pore organization
(GO:0006999)
Nucleocytoplasmic transport
(GO:0006913)
Protein-membrane adaptor activity
(GO:0043495)
Protein binding
(GO:0005515)
Protein export from nucleus
(GO:0006611)
Protein homodimerization activity
(GO:0042803)
Protein import into nucleus
(GO:0006606)
Rna binding
(GO:0003723)
Rna export from nucleus
(GO:0006405)
Rna import into nucleus
(GO:0006404)
Structural constituent of nuclear pore
(GO:0017056)
Tubulin binding
(GO:0015631)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: ependymal cell (CL0000065)
Fold Change: 2.33
Marker Score: 813
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 2.27
Marker Score: 2425
Cell Name: blood cell (CL0000081)
Fold Change: 2.23
Marker Score: 25870
Cell Name: mesodermal cell (CL0000222)
Fold Change: 2.21
Marker Score: 29193
Cell Name: mature T cell (CL0002419)
Fold Change: 2.19
Marker Score: 21717
Cell Name: CD8-positive, alpha-beta cytokine secreting effector T cell (CL0000908)
Fold Change: 2.18
Marker Score: 940
Cell Name: nasal mucosa goblet cell (CL0002480)
Fold Change: 2.17
Marker Score: 1453
Cell Name: oogonial cell (CL0000024)
Fold Change: 2.17
Marker Score: 3112
Cell Name: memory regulatory T cell (CL0002678)
Fold Change: 2.16
Marker Score: 753
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 2.13
Marker Score: 18730
Cell Name: ciliated cell (CL0000064)
Fold Change: 2.13
Marker Score: 7323
Cell Name: basal cell of epithelium of trachea (CL1000348)
Fold Change: 2.1
Marker Score: 15617
Cell Name: Unknown (CL0000548)
Fold Change: 2.09
Marker Score: 1520
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 2.06
Marker Score: 492
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 2.05
Marker Score: 13352
Cell Name: mature alpha-beta T cell (CL0000791)
Fold Change: 2.04
Marker Score: 108088
Cell Name: cell in vitro (CL0001034)
Fold Change: 2.04
Marker Score: 70782
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 2.02
Marker Score: 22695
Cell Name: fraction A pre-pro B cell (CL0002045)
Fold Change: 1.99
Marker Score: 2008
Cell Name: granulosa cell (CL0000501)
Fold Change: 1.99
Marker Score: 20032
Cell Name: basal cell (CL0000646)
Fold Change: 1.99
Marker Score: 2568
Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
Fold Change: 1.99
Marker Score: 17277
Cell Name: type I NK T cell (CL0000921)
Fold Change: 1.98
Marker Score: 1554
Cell Name: ovarian surface epithelial cell (CL2000064)
Fold Change: 1.97
Marker Score: 5368
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.96
Marker Score: 2892
Cell Name: neural crest cell (CL0011012)
Fold Change: 1.96
Marker Score: 2093
Cell Name: epithelial cell of lower respiratory tract (CL0002632)
Fold Change: 1.95
Marker Score: 8117.5
Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.94
Marker Score: 19683
Cell Name: migratory enteric neural crest cell (CL0002607)
Fold Change: 1.94
Marker Score: 1825
Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
Fold Change: 1.93
Marker Score: 5409
Cell Name: Unknown (CL0002371)
Fold Change: 1.91
Marker Score: 2034
Cell Name: large pre-B-II cell (CL0000957)
Fold Change: 1.91
Marker Score: 5201
Cell Name: hematopoietic stem cell (CL0000037)
Fold Change: 1.91
Marker Score: 1005
Cell Name: cortical thymic epithelial cell (CL0002364)
Fold Change: 1.9
Marker Score: 7040
Cell Name: Bergmann glial cell (CL0000644)
Fold Change: 1.89
Marker Score: 770
Cell Name: enteric smooth muscle cell (CL0002504)
Fold Change: 1.89
Marker Score: 4442.5
Cell Name: pro-B cell (CL0000826)
Fold Change: 1.89
Marker Score: 1821
Cell Name: CD4-positive helper T cell (CL0000492)
Fold Change: 1.88
Marker Score: 2042
Cell Name: CD34-positive, CD38-negative hematopoietic stem cell (CL0001024)
Fold Change: 1.88
Marker Score: 1358
Cell Name: supporting cell (CL0000630)
Fold Change: 1.87
Marker Score: 3517
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 1.87
Marker Score: 1967
Cell Name: erythroblast (CL0000765)
Fold Change: 1.86
Marker Score: 1164
Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
Fold Change: 1.86
Marker Score: 1167
Cell Name: bronchus fibroblast of lung (CL2000093)
Fold Change: 1.85
Marker Score: 2542
Cell Name: alpha-beta T cell (CL0000789)
Fold Change: 1.85
Marker Score: 1398
Cell Name: adventitial cell (CL0002503)
Fold Change: 1.84
Marker Score: 455
Cell Name: epithelial cell of nephron (CL1000449)
Fold Change: 1.84
Marker Score: 3839
Cell Name: myeloid leukocyte (CL0000766)
Fold Change: 1.84
Marker Score: 2219
Cell Name: pro-T cell (CL0000827)
Fold Change: 1.83
Marker Score: 7489
Cell Name: naive regulatory T cell (CL0002677)
Fold Change: 1.82
Marker Score: 554
Cell Name: mononuclear phagocyte (CL0000113)
Fold Change: 1.82
Marker Score: 1832
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 1.82
Marker Score: 7164
Cell Name: hepatocyte (CL0000182)
Fold Change: 1.82
Marker Score: 1244
Cell Name: central memory CD8-positive, alpha-beta T cell (CL0000907)
Fold Change: 1.82
Marker Score: 4432
Cell Name: melanocyte (CL0000148)
Fold Change: 1.81
Marker Score: 735
Cell Name: B-1 B cell (CL0000819)
Fold Change: 1.81
Marker Score: 3162
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 1.81
Marker Score: 3074
Cell Name: double negative T regulatory cell (CL0011024)
Fold Change: 1.79
Marker Score: 1730
Cell Name: mesothelial cell of epicardium (CL0011019)
Fold Change: 1.78
Marker Score: 572
Cell Name: plasmablast (CL0000980)
Fold Change: 1.78
Marker Score: 2368
Cell Name: acinar cell (CL0000622)
Fold Change: 1.78
Marker Score: 1253
Cell Name: Sertoli cell (CL0000216)
Fold Change: 1.77
Marker Score: 10502
Cell Name: Leydig cell (CL0000178)
Fold Change: 1.77
Marker Score: 1908
Cell Name: erythroid progenitor cell, mammalian (CL0001066)
Fold Change: 1.76
Marker Score: 564
Cell Name: effector CD4-positive, alpha-beta T cell (CL0001044)
Fold Change: 1.76
Marker Score: 1645
Cell Name: endothelial cell of uterus (CL0009095)
Fold Change: 1.75
Marker Score: 3505
Cell Name: memory B cell (CL0000787)
Fold Change: 1.75
Marker Score: 1326
Cell Name: DN3 thymocyte (CL0000807)
Fold Change: 1.74
Marker Score: 870
Cell Name: hematopoietic multipotent progenitor cell (CL0000837)
Fold Change: 1.74
Marker Score: 849
Cell Name: fibroblast of breast (CL4006000)
Fold Change: 1.74
Marker Score: 990
Cell Name: gamma-delta T cell (CL0000798)
Fold Change: 1.73
Marker Score: 1165
Cell Name: T-helper 22 cell (CL0001042)
Fold Change: 1.73
Marker Score: 7408
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 1.72
Marker Score: 58669
Cell Name: papillary tips cell (CL1000597)
Fold Change: 1.72
Marker Score: 348
Cell Name: respiratory epithelial cell (CL0002368)
Fold Change: 1.72
Marker Score: 949
Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
Fold Change: 1.72
Marker Score: 1460
Cell Name: innate lymphoid cell (CL0001065)
Fold Change: 1.72
Marker Score: 617
Cell Name: glial cell (CL0000125)
Fold Change: 1.71
Marker Score: 1884
Cell Name: regulatory T cell (CL0000815)
Fold Change: 1.71
Marker Score: 1892
Cell Name: mature NK T cell (CL0000814)
Fold Change: 1.71
Marker Score: 790
Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
Fold Change: 1.7
Marker Score: 373
Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
Fold Change: 1.7
Marker Score: 710
Cell Name: early lymphoid progenitor (CL0000936)
Fold Change: 1.7
Marker Score: 831
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: 1.69
Marker Score: 3002
Cell Name: parietal cell (CL0000162)
Fold Change: 1.69
Marker Score: 472
Cell Name: choroid plexus epithelial cell (CL0000706)
Fold Change: 1.69
Marker Score: 1555
Cell Name: leukocyte (CL0000738)
Fold Change: 1.69
Marker Score: 971
Cell Name: promonocyte (CL0000559)
Fold Change: 1.69
Marker Score: 1090
Cell Name: double-positive, alpha-beta thymocyte (CL0000809)
Fold Change: 1.69
Marker Score: 3313
Cell Name: primordial germ cell (CL0000670)
Fold Change: 1.69
Marker Score: 2119.5
Cell Name: mature gamma-delta T cell (CL0000800)
Fold Change: 1.69
Marker Score: 5319
Cell Name: mesenchymal stem cell (CL0000134)
Fold Change: 1.68
Marker Score: 2593
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 1.68
Marker Score: 4991
Cell Name: starburst amacrine cell (CL0004232)
Fold Change: 1.68
Marker Score: 477
Cell Name: epithelial cell of uterus (CL0002149)
Fold Change: 1.68
Marker Score: 385
Cell Name: T follicular helper cell (CL0002038)
Fold Change: 1.68
Marker Score: 1395
Cell Name: bronchial epithelial cell (CL0002328)
Fold Change: 1.67
Marker Score: 443
Cell Name: taste receptor cell (CL0000209)
Fold Change: 1.67
Marker Score: 1445
Cell Name: Schwann cell (CL0002573)
Fold Change: 1.67
Marker Score: 580
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 1.67
Marker Score: 476

Hover over a box to see details here...

**Key Characteristics** The TPR gene is characterized by its unique structure, which consists of a translocated promoter region and a nuclear basket protein domain. This domain is involved in the regulation of chromatin binding, nuclear envelope breakdown, and nuclear pore complex disassembly. The TPR protein is also known to interact with various host cellular proteins, including heat shock proteins, cytokines, and viral proteins. These interactions play a crucial role in regulating the expression of genes involved in antiviral mechanisms, cell cycle regulation, and immune responses. **Pathways and Functions** The TPR gene is involved in several key pathways, including: 1. **Antiviral Mechanisms**: The TPR protein is involved in the regulation of interferon-stimulated genes, which play a crucial role in the host's defense against viral infections. 2. **Cell Cycle Regulation**: The TPR protein is involved in the regulation of the cell cycle, particularly in the context of mitotic prophase and the nuclear envelope breakdown. 3. **Immune Responses**: The TPR protein is involved in the regulation of cytokine signaling, which is crucial for the activation of immune cells and the induction of immune responses. 4. **Heat Shock Response**: The TPR protein is involved in the regulation of the heat shock response, which is a critical response to cellular stress. 5. **Viral Infection Pathways**: The TPR protein is involved in the regulation of viral infection pathways, including the export of viral ribonucleoproteins from the nucleus. **Clinical Significance** The TPR gene has been implicated in several diseases, including: 1. **Thyroid Papillary Carcinoma**: Defective TPR may confer susceptibility towards thyroid papillary carcinoma. 2. **HIV Infection**: The TPR protein is involved in the regulation of HIV infection pathways, including the export of viral ribonucleoproteins from the nucleus. 3. **SARS-CoV-2 Infection**: The TPR protein is involved in the regulation of SARS-CoV-2-host interactions, including the activation of innate and adaptive immune responses. 4. **Cancer**: The TPR protein is involved in the regulation of signaling pathways that are critical for cancer development and progression. In conclusion, the TPR gene plays a crucial role in various cellular processes, including antiviral mechanisms, cell cycle regulation, and immune responses. Its dysregulation has been implicated in several diseases, including thyroid papillary carcinoma, HIV infection, and SARS-CoV-2 infection. Further research is needed to fully understand the function of the TPR gene and its role in human disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Nucleoprotein TPR

Genular Protein ID: 3579207324

Symbol: TPR_HUMAN

Name: Nucleoprotein TPR

UniProtKB Accession Codes:

P12270 Q15624 Q15655 Q5SWY0 Q99968

Database IDs:

Citations:

PubMed ID: 1549355

Title: Nucleotide sequence analysis of human tpr cDNA clones.

PubMed ID: 1549355

PubMed ID: 1437155

Title: The human tpr gene encodes a protein of 2094 amino acids that has extensive coiled-coil regions and an acidic C-terminal domain.

PubMed ID: 1437155

PubMed ID: 7798308

Title: Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex.

PubMed ID: 7798308

DOI: 10.1083/jcb.127.6.1515

PubMed ID: 9024684

Title: Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments.

PubMed ID: 9024684

DOI: 10.1083/jcb.136.3.515

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 1532241

Title: TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes in human papillary thyroid carcinomas.

PubMed ID: 1532241

PubMed ID: 3387099

Title: tpr homologues activate met and raf.

PubMed ID: 3387099

PubMed ID: 2300559

Title: TPR-MET oncogenic rearrangement: detection by polymerase chain reaction amplification of the transcript and expression in human tumor cell lines.

PubMed ID: 2300559

DOI: 10.1073/pnas.87.2.738

PubMed ID: 9828100

Title: Molecular segments of protein Tpr that confer nuclear targeting and association with the nuclear pore complex.

PubMed ID: 9828100

DOI: 10.1006/excr.1998.4246

PubMed ID: 9864356

Title: Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export.

PubMed ID: 9864356

DOI: 10.1083/jcb.143.7.1801

PubMed ID: 11514627

Title: Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to the nuclear pore complex but not parallel, in-register homodimerization.

PubMed ID: 11514627

DOI: 10.1091/mbc.12.8.2433

PubMed ID: 12424524

Title: The evolutionarily conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes.

PubMed ID: 12424524

DOI: 10.1007/s00412-002-0208-2

PubMed ID: 11952838

Title: Nucleocytoplasmic transport of proteins and poly(A)+ RNA in reconstituted Tpr-less nuclei in living mammalian cells.

PubMed ID: 11952838

DOI: 10.1046/j.1365-2443.2002.00525.x

PubMed ID: 11839768

Title: Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export.

PubMed ID: 11839768

DOI: 10.1083/jcb.200106046

PubMed ID: 12802065

Title: Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.

PubMed ID: 12802065

DOI: 10.1091/mbc.e02-09-0620

PubMed ID: 15229283

Title: Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.

PubMed ID: 15229283

DOI: 10.1091/mbc.e04-03-0165

PubMed ID: 15654337

Title: Polyglutamine expansion of huntingtin impairs its nuclear export.

PubMed ID: 15654337

DOI: 10.1038/ng1503

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17897941

Title: HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA.

PubMed ID: 17897941

DOI: 10.1074/jbc.m704054200

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18981471

Title: Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint.

PubMed ID: 18981471

DOI: 10.1101/gad.1677208

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18794356

Title: Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and docking domain on the nuclear pore complex protein Tpr cooperatively regulate ERK2-Tpr interaction.

PubMed ID: 18794356

DOI: 10.1128/mcb.00925-08

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19835572

Title: Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr.

PubMed ID: 19835572

DOI: 10.1186/1471-2121-10-74

PubMed ID: 19273613

Title: Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator.

PubMed ID: 19273613

DOI: 10.1083/jcb.200811012

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20407419

Title: Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.

PubMed ID: 20407419

DOI: 10.1038/emboj.2010.54

PubMed ID: 20133940

Title: Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis.

PubMed ID: 20133940

DOI: 10.1074/jbc.m110.105890

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21613532

Title: The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway.

PubMed ID: 21613532

DOI: 10.1261/rna.2616111

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22253824

Title: Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.

PubMed ID: 22253824

DOI: 10.1371/journal.pone.0029921

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 24970816

Title: The subcellular distribution and function of MTA1 in cancer differentiation.

PubMed ID: 24970816

DOI: 10.18632/oncotarget.2095

PubMed ID: 34494102

Title: Pathogenic variants in nucleoporin TPR (translocated promoter region, nuclear basket protein) cause severe intellectual disability in humans.

PubMed ID: 34494102

DOI: 10.1093/hmg/ddab248

Sequence Information:

Length: 2363
Mass: 267293
Checksum: 01E669CBDC496772
Sequence:

MAAVLQQVLE RTELNKLPKS VQNKLEKFLA DQQSEIDGLK GRHEKFKVES EQQYFEIEKR 
LSHSQERLVN ETRECQSLRL ELEKLNNQLK ALTEKNKELE IAQDRNIAIQ SQFTRTKEEL 
EAEKRDLIRT NERLSQELEY LTEDVKRLNE KLKESNTTKG ELQLKLDELQ ASDVSVKYRE 
KRLEQEKELL HSQNTWLNTE LKTKTDELLA LGREKGNEIL ELKCNLENKK EEVSRLEEQM 
NGLKTSNEHL QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS 
NELTRAVEEL HKLLKEAGEA NKAIQDHLLE VEQSKDQMEK EMLEKIGRLE KELENANDLL 
SATKRKGAIL SEEELAAMSP TAAAVAKIVK PGMKLTELYN AYVETQDQLL LEKLENKRIN 
KYLDEIVKEV EAKAPILKRQ REEYERAQKA VASLSVKLEQ AMKEIQRLQE DTDKANKQSS 
VLERDNRRME IQVKDLSQQI RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY 
RNIEELQQQN QRLLVALREL GETREREEQE TTSSKITELQ LKLESALTEL EQLRKSRQHQ 
MQLVDSIVRQ RDMYRILLSQ TTGVAIPLHA SSLDDVSLAS TPKRPSTSQT VSTPAPVPVI 
ESTEAIEAKA ALKQLQEIFE NYKKEKAENE KIQNEQLEKL QEQVTDLRSQ NTKISTQLDF 
ASKRYEMLQD NVEGYRREIT SLHERNQKLT ATTQKQEQII NTMTQDLRGA NEKLAVAEVR 
AENLKKEKEM LKLSEVRLSQ QRESLLAEQR GQNLLLTNLQ TIQGILERSE TETKQRLSSQ 
IEKLEHEISH LKKKLENEVE QRHTLTRNLD VQLLDTKRQL DTETNLHLNT KELLKNAQKE 
IATLKQHLSN MEVQVASQSS QRTGKGQPSN KEDVDDLVSQ LRQTEEQVND LKERLKTSTS 
NVEQYQAMVT SLEESLNKEK QVTEEVRKNI EVRLKESAEF QTQLEKKLME VEKEKQELQD 
DKRRAIESME QQLSELKKTL SSVQNEVQEA LQRASTALSN EQQARRDCQE QAKIAVEAQN 
KYERELMLHA ADVEALQAAK EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERMLKD 
EVSKCVCRCE DLEKQNRLLH DQIEKLSDKV VASVKEGVQG PLNVSLSEEG KSQEQILEIL 
RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ VTAKTMAQHE 
ELMKKTETMN VVMETNKMLR EEKERLEQDL QQMQAKVRKL ELDILPLQEA NAELSEKSGM 
LQAEKKLLEE DVKRWKARNQ HLVSQQKDPD TEEYRKLLSE KEVHTKRIQQ LTEEIGRLKA 
EIARSNASLT NNQNLIQSLK EDLNKVRTEK ETIQKDLDAK IIDIQEKVKT ITQVKKIGRR 
YKTQYEELKA QQDKVMETSA QSSGDHQEQH VSVQEMQELK ETLNQAETKS KSLESQVENL 
QKTLSEKETE ARNLQEQTVQ LQSELSRLRQ DLQDRTTQEE QLRQQITEKE EKTRKAIVAA 
KSKIAHLAGV KDQLTKENEE LKQRNGALDQ QKDELDVRIT ALKSQYEGRI SRLERELREH 
QERHLEQRDE PQEPSNKVPE QQRQITLKTT PASGERGIAS TSDPPTANIK PTPVVSTPSK 
VTAAAMAGNK STPRASIRPM VTPATVTNPT TTPTATVMPT TQVESQEAMQ SEGPVEHVPV 
FGSTSGSVRS TSPNVQPSIS QPILTVQQQT QATAFVQPTQ QSHPQIEPAN QELSSNIVEV 
VQSSPVERPS TSTAVFGTVS ATPSSSLPKR TREEEEDSTI EASDQVSDDT VEMPLPKKLK 
SVTPVGTEEE VMAEESTDGE VETQVYNQDS QDSIGEGVTQ GDYTPMEDSE ETSQSLQIDL 
GPLQSDQQTT TSSQDGQGKG DDVIVIDSDD EEEDDDENDG EHEDYEEDEE DDDDDEDDTG 
MGDEGEDSNE GTGSADGNDG YEADDAEGGD GTDPGTETEE SMGGGEGNHR AADSQNSGEG 
NTGAAESSFS QEVSREQQPS SASERQAPRA PQSPRRPPHP LPPRLTIHAP PQELGPPVQR 
IQMTRRQSVG RGLQLTPGIG GMQQHFFDDE DRTVPSTPTL VVPHRTDGFA EAIHSPQVAG 
VPRFRFGPPE DMPQTSSSHS DLGQLASQGG LGMYETPLFL AHEEESGGRS VPTTPLQVAA 
PVTVFTESTT SDASEHASQS VPMVTTSTGT LSTTNETATG DDGDEVFVEA ESEGISSEAG 
LEIDSQQEEE PVQASDESDL PSTSQDPPSS SSVDTSSSQP KPFRRVRLQT TLRQGVRGRQ 
FNRQRGVSHA MGGRGGINRG NIN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: TPR

Associated with

Cells (max top 100)

Other Information

Nucleotide sequence analysis of human tpr cDNA clones. PubMed ID: 1549355

The human tpr gene encodes a protein of 2094 amino acids that has extensive coiled-coil regions and an acidic C-terminal domain. PubMed ID: 1437155

Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. PubMed ID: 7798308

Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. PubMed ID: 9024684

The DNA sequence and biological annotation of human chromosome 1. PubMed ID: 16710414

TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes in human papillary thyroid carcinomas. PubMed ID: 1532241

tpr homologues activate met and raf. PubMed ID: 3387099

TPR-MET oncogenic rearrangement: detection by polymerase chain reaction amplification of the transcript and expression in human tumor cell lines. PubMed ID: 2300559

Molecular segments of protein Tpr that confer nuclear targeting and association with the nuclear pore complex. PubMed ID: 9828100

Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export. PubMed ID: 9864356

Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to the nuclear pore complex but not parallel, in-register homodimerization. PubMed ID: 11514627

The evolutionarily conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes. PubMed ID: 12424524

Nucleocytoplasmic transport of proteins and poly(A)+ RNA in reconstituted Tpr-less nuclei in living mammalian cells. PubMed ID: 11952838

Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. PubMed ID: 11839768

Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex. PubMed ID: 12802065

Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. PubMed ID: 15229283

Polyglutamine expansion of huntingtin impairs its nuclear export. PubMed ID: 15654337

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA. PubMed ID: 17897941

Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. PubMed ID: 17924679

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PubMed ID: 17525332

Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint. PubMed ID: 18981471

Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PubMed ID: 18220336

Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and docking domain on the nuclear pore complex protein Tpr cooperatively regulate ERK2-Tpr interaction. PubMed ID: 18794356

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr. PubMed ID: 19835572

Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator. PubMed ID: 19273613

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion. PubMed ID: 20407419

Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis. PubMed ID: 20133940

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway. PubMed ID: 21613532

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA. PubMed ID: 22253824

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

The subcellular distribution and function of MTA1 in cancer differentiation. PubMed ID: 24970816

Pathogenic variants in nucleoporin TPR (translocated promoter region, nuclear basket protein) cause severe intellectual disability in humans. PubMed ID: 34494102